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07-095

Sigma-Aldrich

Anti-PP2A-methylesterase/PME-1 Antibody

Upstate®, from rabbit

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About This Item

Código UNSPSC:
12352203
eCl@ss:
32160702
NACRES:
NA.41

origen biológico

rabbit

Nivel de calidad

forma del anticuerpo

purified immunoglobulin

tipo de anticuerpo

primary antibodies

clon

polyclonal

reactividad de especies

human, rat, mouse

fabricante / nombre comercial

Upstate®

técnicas

western blot: suitable

isotipo

IgG

Nº de acceso NCBI

Nº de acceso UniProt

Condiciones de envío

dry ice

modificación del objetivo postraduccional

unmodified

Información sobre el gen

human ... PPME1(51400)

Especificidad

Protein Phosphatase Methylesterase-1

Inmunógeno

A mixture of two nickel agarose-purified, His6-tagged, bacterial expressed human Protein Phosphatase Methylesterase-1 (PME-1) fragments (residues 225-302 and 277-387). These two fragments represent the carboxyl-terminal portion of the protein.

Aplicación

Research Category
Signaling

Neuroscience
Research Sub Category
Neurotransmitters & Receptors

Neurodegenerative Diseases
This Anti-PP2A-methylesterase/PME-1 Antibody is validated for use in IP, WB for the detection of PP2A-methylesterase/PME-1.

Calidad

routinely evaluated by immunoblot on RIPA lysates from mouse 3T3 fibroblasts

Descripción de destino

44kDa

Forma física

0.1M Tris-glycine, pH 7.4, 0.15M NaCl, 0.05% sodium azide before the addition of glycerol to 30%
Format: Purified
Protein A chromatography

Almacenamiento y estabilidad

2 years at -20°C

Nota de análisis

Control
Positive Antigen Control: Catalog #12-305, 3T3/A31 lysate. Add 2.5 μL of 2-mercapto-ethanol/100 μL of lysate and boil for 5 minutes to reduce the preparation. Load 20 μg of reduced lysate per lane for minigels.

Información legal

UPSTATE is a registered trademark of Merck KGaA, Darmstadt, Germany

Cláusula de descargo de responsabilidad

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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Código de clase de almacenamiento

10 - Combustible liquids

Clase de riesgo para el agua (WGK)

WGK 1


Certificados de análisis (COA)

Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»

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Single-pot enzymatic synthesis of Dicer-substrate siRNAs.
Guiley, KZ; Pratt, AJ; MacRae, IJ
Nucleic Acids Research null
Madhumathi Gnanaprakash et al.
Journal of Alzheimer's disease : JAD, 79(4), 1813-1829 (2021-01-19)
The serine/threonine protein phosphatase, PP2A, is thought to play a central role in the molecular pathogenesis of Alzheimer's disease (AD), and the activity and substrate specificity of PP2A is regulated, in part, through methylation and demethylation of its catalytic subunit.
Christina Ising et al.
Nature, 575(7784), 669-673 (2019-11-22)
Alzheimer's disease is characterized by the accumulation of amyloid-beta in plaques, aggregation of hyperphosphorylated tau in neurofibrillary tangles and neuroinflammation, together resulting in neurodegeneration and cognitive decline1. The NLRP3 inflammasome assembles inside of microglia on activation, leading to increased cleavage
Ha Yin Lee et al.
Science signaling, 11(512) (2018-01-11)
Cancer cells increase glucose metabolism to support aerobic glycolysis. However, only some cancer cells are acutely sensitive to glucose withdrawal, and the underlying mechanism of this selective sensitivity is unclear. We showed that glucose deprivation initiates a cell death pathway
Kesava Asam et al.
PloS one, 12(12), e0189413-e0189413 (2017-12-19)
Soluble forms of oligomeric beta-amyloid (Aβ) are thought to play a central role in Alzheimer's disease (AD). Transgenic manipulation of methylation of the serine/threonine protein phosphatase, PP2A, was recently shown to alter the sensitivity of mice to AD-related impairments resulting

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